메뉴 건너뛰기




Volumn 15, Issue 11, 1997, Pages 1174-1182

Synthesis of α-gal epitopes on influenza virus vaccines, by recombinant α1,3galactosyltransferase, enables the formation of immune complexes with the natural anti-Gal antibody

Author keywords

1,3galactosyltransferase; gal epitope; Anti Gal; Influenza virus

Indexed keywords

ANTIBODY; EPITOPE; GALACTOSE; GALACTOSYLTRANSFERASE; INFLUENZA VACCINE; RECOMBINANT GALACTOSYLTRANSFERASE; UNCLASSIFIED DRUG; VIRUS HEMAGGLUTININ;

EID: 0030829012     PISSN: 0264410X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0264-410X(96)00300-3     Document Type: Article
Times cited : (29)

References (44)
  • 1
    • 0023217305 scopus 로고
    • Modulation of the immunological response to hepatitis B virus by antibodies
    • Celis, E., Abraham, K.G. and Miller, R.W. Modulation of the immunological response to hepatitis B virus by antibodies. Hepatology 1987, 7, 563-568.
    • (1987) Hepatology , vol.7 , pp. 563-568
    • Celis, E.1    Abraham, K.G.2    Miller, R.W.3
  • 2
    • 0017328961 scopus 로고
    • Inactivated Venezuelan equine encephalomyelitis virus vaccine complexed with specific antibody: Enhanced primary immune response and altered pattern of antibody class elicited
    • Houston, W.E., Kremer, R.J., Crabbs, C.L. and Spertzel, R.O. Inactivated Venezuelan equine encephalomyelitis virus vaccine complexed with specific antibody: enhanced primary immune response and altered pattern of antibody class elicited. J. Infect. Dis. 1977, 7, 600-610.
    • (1977) J. Infect. Dis. , vol.7 , pp. 600-610
    • Houston, W.E.1    Kremer, R.J.2    Crabbs, C.L.3    Spertzel, R.O.4
  • 3
    • 0021343233 scopus 로고
    • Antibodies to hepatitis B surface antigen potentiate the response of human T lymphocyte clones to the same antigen
    • Celis, E. and Chang, T.W. Antibodies to hepatitis B surface antigen potentiate the response of human T lymphocyte clones to the same antigen. Science 1984, 224, 297-299.
    • (1984) Science , vol.224 , pp. 297-299
    • Celis, E.1    Chang, T.W.2
  • 4
    • 0026017326 scopus 로고
    • Effect of antigen/antibody ratio on macrophage uptake, processing and presentation to T cells of antigen complexed with polyclonal antibodies
    • Manca, F., Fenoglio, D., LiPira, G., Kunkl, A. and Celada, F. Effect of antigen/antibody ratio on macrophage uptake, processing and presentation to T cells of antigen complexed with polyclonal antibodies. J. Exp. Med. 1991, 173, 37-48.
    • (1991) J. Exp. Med. , vol.173 , pp. 37-48
    • Manca, F.1    Fenoglio, D.2    LiPira, G.3    Kunkl, A.4    Celada, F.5
  • 5
    • 0026445735 scopus 로고
    • Enhanced antigen presentation using human Fcγ receptor (monocyte/macrophage)-specific immunogens
    • Gosselin, E.J., Wardwell, K., Gosselin, D.R., Alter, N., Fisher, J.L. and Guyre, P. Enhanced antigen presentation using human Fcγ receptor (monocyte/macrophage)-specific immunogens. J. Immunol. 1992, 149, 3477-3481.
    • (1992) J. Immunol. , vol.149 , pp. 3477-3481
    • Gosselin, E.J.1    Wardwell, K.2    Gosselin, D.R.3    Alter, N.4    Fisher, J.L.5    Guyre, P.6
  • 6
    • 0030049224 scopus 로고    scopus 로고
    • FcγRII on human B cells can mediate enhanced antigen presentation
    • Liu, C., Gosselin, E. and Guyre, P. FcγRII on human B cells can mediate enhanced antigen presentation. Cell. Immunol. 1996, 167, 188-194.
    • (1996) Cell. Immunol. , vol.167 , pp. 188-194
    • Liu, C.1    Gosselin, E.2    Guyre, P.3
  • 7
    • 0028289244 scopus 로고
    • Efficient presentation of soluble antigen by cultured human dendritic cells is maintained by granulocyte/macrophage colony stimulating factor plus Interleukin 4 and down regulated by tumor necrosis factor α
    • Sallusto, F. and Lanzavecchia, A. Efficient presentation of soluble antigen by cultured human dendritic cells is maintained by granulocyte/macrophage colony stimulating factor plus Interleukin 4 and down regulated by tumor necrosis factor α. J. Exp. Med. 1994, 179, 1109-1112.
    • (1994) J. Exp. Med. , vol.179 , pp. 1109-1112
    • Sallusto, F.1    Lanzavecchia, A.2
  • 8
    • 0029958448 scopus 로고    scopus 로고
    • Type I (CD64) and Type II (CD32) Fc receptor-mediated phagocytosis by human blood dendritic cells
    • Fanger, N.A., Wardwell, K., Shen, L., Tedder, T.F. and Guyre, P.M. Type I (CD64) and Type II (CD32) Fc receptor-mediated phagocytosis by human blood dendritic cells. J. Immunol. 1996, 157, 541-548.
    • (1996) J. Immunol. , vol.157 , pp. 541-548
    • Fanger, N.A.1    Wardwell, K.2    Shen, L.3    Tedder, T.F.4    Guyre, P.M.5
  • 9
    • 0021678856 scopus 로고
    • A unique natural human IgG antibody with anti-α-Galactosyl specificity
    • Galili, U., Rachmilewitz, E.A., Peleg, A. and Flechner, I. A unique natural human IgG antibody with anti-α-Galactosyl specificity. J. Exp. Med. 1984, 160, 1519-1531.
    • (1984) J. Exp. Med. , vol.160 , pp. 1519-1531
    • Galili, U.1    Rachmilewitz, E.A.2    Peleg, A.3    Flechner, I.4
  • 10
    • 0027295654 scopus 로고
    • Evolution and pathophysiology of the human natural anti-Gal antibody
    • Galili, U. Evolution and pathophysiology of the human natural anti-Gal antibody. Springer Semin. Immunopathol. 1993, 15, 155-171.
    • (1993) Springer Semin. Immunopathol. , vol.15 , pp. 155-171
    • Galili, U.1
  • 11
    • 0022260876 scopus 로고
    • Human natural anti-α-Galactosyl IgG. II. The specific recognition of α(1→3)-linked galactose residues
    • Galili, U., Macher, B.A., Buehler, J. and Shohet, S.B. Human natural anti-α-Galactosyl IgG. II. The specific recognition of α(1→3)-linked galactose residues. J. Exp. Med. 1985, 162, 573-582.
    • (1985) J. Exp. Med. , vol.162 , pp. 573-582
    • Galili, U.1    Macher, B.A.2    Buehler, J.3    Shohet, S.B.4
  • 12
    • 0023276640 scopus 로고
    • The human natural anti-Gal IgG. III. The subtlety of immune tolerance in man as demonstrated by crossreactivity between natural anti-Gal and anti-B antibodies
    • Galili, U., Buehler, J., Shohet, S.B. and Macher, B.A. The human natural anti-Gal IgG. III. The subtlety of immune tolerance in man as demonstrated by crossreactivity between natural anti-Gal and anti-B antibodies. J. Exp. Med. 1987, 165, 693-704.
    • (1987) J. Exp. Med. , vol.165 , pp. 693-704
    • Galili, U.1    Buehler, J.2    Shohet, S.B.3    Macher, B.A.4
  • 13
    • 0000665022 scopus 로고
    • Evolutionary relationship between the anti-Gal antibody and the Galα1→3Gal epitope in primates
    • Galili, U., Clark, M.R., Shohet, S.B., Buehler, J. and Macher, B.A. Evolutionary relationship between the anti-Gal antibody and the Galα1→3Gal epitope in primates. Proc. Natl Acad. Sci. USA 1987, 84, 1369-1373.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 1369-1373
    • Galili, U.1    Clark, M.R.2    Shohet, S.B.3    Buehler, J.4    Macher, B.A.5
  • 14
    • 0024297335 scopus 로고
    • Man, apes, and Old World monkeys differ from other mammals in the expression of α-Galactosyl epitopes on nucleated cells
    • Galili, U., Shohet, S.B., Kobrin, E., Stults, C.L.M. and Macher, B.A. Man, apes, and Old World monkeys differ from other mammals in the expression of α-Galactosyl epitopes on nucleated cells. J. Biol. Chem. 1988, 263, 17755-17762.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17755-17762
    • Galili, U.1    Shohet, S.B.2    Kobrin, E.3    Stults, C.L.M.4    Macher, B.A.5
  • 16
    • 0028268967 scopus 로고
    • Differential host dependent expression of α-Galactosyl epitopes on viral glycoproteins: A study on eastern equine encephalitis virs as a model
    • Repik, P.M., Strizki, J.M. and Galili, U. Differential host dependent expression of α-Galactosyl epitopes on viral glycoproteins: a study on eastern equine encephalitis virs as a model. J. Gen. Virol. 1994, 75, 1177-1181.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1177-1181
    • Repik, P.M.1    Strizki, J.M.2    Galili, U.3
  • 17
    • 0028804822 scopus 로고
    • A novel mechanism of retrovirus inactivation in human serum mediated by α-Galactosyl natural antibody
    • Rother, R.P., Fodor, W.L. and Springhorn, J.P. et al. A novel mechanism of retrovirus inactivation in human serum mediated by α-Galactosyl natural antibody. J. Exp. Med. 1995, 18, 1345-1355.
    • (1995) J. Exp. Med. , vol.18 , pp. 1345-1355
    • Rother, R.P.1    Fodor, W.L.2    Springhorn, J.P.3
  • 18
    • 0030070191 scopus 로고    scopus 로고
    • Sensitization of cells and retroviruses to human serum b α1 ,3galactosyltransferase
    • Takeuchi, Y., Porter, C.D. and Strahan, K.M. et al. Sensitization of cells and retroviruses to human serum b α1 ,3galactosyltransferase. Nature 1996, 379, 85-88.
    • (1996) Nature , vol.379 , pp. 85-88
    • Takeuchi, Y.1    Porter, C.D.2    Strahan, K.M.3
  • 19
    • 0030602795 scopus 로고    scopus 로고
    • The α-Galactosyl epitope: A sugar coating that makes viruses and cells unpalatable
    • Rother, R.P. and Squinto, S.P. The α-Galactosyl epitope: a sugar coating that makes viruses and cells unpalatable. Cell 1996, 86, 185-188.
    • (1996) Cell , vol.86 , pp. 185-188
    • Rother, R.P.1    Squinto, S.P.2
  • 20
    • 0029978369 scopus 로고    scopus 로고
    • Enhancement of antigen presentation of influenza virus hemagglutinin by the natural anti-Gal antibody
    • Galili, U., Repik, P.K., Anaraki, F., Mozdzanowska, K., Washko, G. and Gerhard, W. Enhancement of antigen presentation of influenza virus hemagglutinin by the natural anti-Gal antibody. Vaccine 1996, 14, 321-328.
    • (1996) Vaccine , vol.14 , pp. 321-328
    • Galili, U.1    Repik, P.K.2    Anaraki, F.3    Mozdzanowska, K.4    Washko, G.5    Gerhard, W.6
  • 21
    • 0014685667 scopus 로고
    • Failure of inactivated influenza vaccine to protect an aged population
    • D'Alessio, D.J., Cox, P.M. and Dick, E.C. Failure of inactivated influenza vaccine to protect an aged population. J. Am. Med. Assoc. 1969, 210, 485-489.
    • (1969) J. Am. Med. Assoc. , vol.210 , pp. 485-489
    • D'Alessio, D.J.1    Cox, P.M.2    Dick, E.C.3
  • 22
    • 0016852047 scopus 로고
    • Influenza vaccination and mortalility from broncho pneumonia in the elderly
    • Howells, C.H.L., Vesselenova-Jenkins, C.K., Evans, A.D. and James, J. Influenza vaccination and mortalility from broncho pneumonia in the elderly. Lancet 1975, 1, 381-383.
    • (1975) Lancet , vol.1 , pp. 381-383
    • Howells, C.H.L.1    Vesselenova-Jenkins, C.K.2    Evans, A.D.3    James, J.4
  • 24
    • 0028048820 scopus 로고
    • The efficacy and cost effectiveness of vaccinating against influenza among elderly persons living in the community
    • Nichol, K.L., Margolis, K.L., Wuorema, J. and Von Sternberg, T. The efficacy and cost effectiveness of vaccinating against influenza among elderly persons living in the community. N. Engl. J. Med. 1994, 331, 778-784.
    • (1994) N. Engl. J. Med. , vol.331 , pp. 778-784
    • Nichol, K.L.1    Margolis, K.L.2    Wuorema, J.3    Von Sternberg, T.4
  • 25
    • 0010306110 scopus 로고
    • Risks for influenza and repiratory illness in vaccinated elderly
    • Gravenstein, S., Drinka, P.J. and Duthie, E.H. et al. Risks for influenza and repiratory illness in vaccinated elderly. Aging: Immunol. Infect. Dis. 1990, 2, 185-193.
    • (1990) Aging: Immunol. Infect. Dis. , vol.2 , pp. 185-193
    • Gravenstein, S.1    Drinka, P.J.2    Duthie, E.H.3
  • 27
    • 0028230361 scopus 로고
    • Defining the minimal size of catalytically active primate α1,3galactosyltransferase: Structure function studies on the recombinant truncated enzyme
    • Henion, T.R., Macher, B.A., Anaraki, F. and Galili, U. Defining the minimal size of catalytically active primate α1,3galactosyltransferase: structure function studies on the recombinant truncated enzyme. Glycobiology 1994, 4, 193-201.
    • (1994) Glycobiology , vol.4 , pp. 193-201
    • Henion, T.R.1    Macher, B.A.2    Anaraki, F.3    Galili, U.4
  • 28
    • 0016429684 scopus 로고
    • Studies on primary structure of influenza virus hemagglutinin
    • Skehel, J.J. and Waterfield, M.D. Studies on primary structure of influenza virus hemagglutinin. Proc. Natl Acad. Sci. USA 1975, 72, 93-97.
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 93-97
    • Skehel, J.J.1    Waterfield, M.D.2
  • 29
    • 0018537631 scopus 로고
    • Immunochemical studies of the combining sites of two isolectins A4 and B4 isolated from Bandeiraea simplicifolia
    • Wood, C., Kabat, E.A., Murphy, L.A. and Goldstein, I.J. Immunochemical studies of the combining sites of two isolectins A4 and B4 isolated from Bandeiraea simplicifolia. Arch. Biochem. Biophys. 1979, 198, 1-9.
    • (1979) Arch. Biochem. Biophys. , vol.198 , pp. 1-9
    • Wood, C.1    Kabat, E.A.2    Murphy, L.A.3    Goldstein, I.J.4
  • 30
    • 0024260839 scopus 로고
    • The asparagine-linked oligosaccharides on bovine fetuin: Structural analysis of N-glycanase related oligosaccharides by 500-megahertz NMR spectoscopy
    • Green, E.D., Adelt, G., Baenzinger, J.U., Wilson, S. and Van-Halbeck, H. The asparagine-linked oligosaccharides on bovine fetuin: Structural analysis of N-glycanase related oligosaccharides by 500-megahertz NMR spectoscopy. J. Biol. Chem. 1988, 263, 18253-18268.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18253-18268
    • Green, E.D.1    Adelt, G.2    Baenzinger, J.U.3    Wilson, S.4    Van-Halbeck, H.5
  • 31
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked carbohydrate chains
    • Kornfeld, R. and Kornfeld, S. Assembly of asparagine-linked carbohydrate chains. Ann. Rev. Biochem. 1985, 54, 631-664.
    • (1985) Ann. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 32
    • 0022137782 scopus 로고
    • Carbohydrates of influenza virus. Structure elucidation of the individual glycans of the FPV hemagglutinin by two-dimensional H NMR and methylation analysis
    • Kiel, W., Geyer, R. and Dabrowski, J. et al. Carbohydrates of influenza virus. Structure elucidation of the individual glycans of the FPV hemagglutinin by two-dimensional H NMR and methylation analysis. EMBO JI. 1985, 4, 2711-2720.
    • (1985) EMBO JI , vol.4 , pp. 2711-2720
    • Kiel, W.1    Geyer, R.2    Dabrowski, J.3
  • 33
    • 0020673992 scopus 로고
    • Carbohydrates of influenza virus hemagglutinin: Structure of the whole neutral sugar chain
    • Matsumoto, A., Yoshima, H. and Kobata, A. Carbohydrates of influenza virus hemagglutinin: structure of the whole neutral sugar chain. Biochemistry 1983, 22, 188-196.
    • (1983) Biochemistry , vol.22 , pp. 188-196
    • Matsumoto, A.1    Yoshima, H.2    Kobata, A.3
  • 35
    • 0024589985 scopus 로고
    • Functional heterogeneity of human Fc receptors for immunoglobulin G
    • Unkeless, J.C. Functional heterogeneity of human Fc receptors for immunoglobulin G. J. Clin. Invest. 1989, 83, 355-361.
    • (1989) J. Clin. Invest. , vol.83 , pp. 355-361
    • Unkeless, J.C.1
  • 36
    • 0025282253 scopus 로고
    • Human epidermal Langerhans cells express only trhe 40-kilodalton Fcγ receptor (FcRII)
    • Schmitt, D.A., Hanan, D. and Bieber, T. et al. Human epidermal Langerhans cells express only trhe 40-kilodalton Fcγ receptor (FcRII). J. Immunol. 1990, 144, 4284-4290.
    • (1990) J. Immunol. , vol.144 , pp. 4284-4290
    • Schmitt, D.A.1    Hanan, D.2    Bieber, T.3
  • 37
    • 0024490847 scopus 로고
    • Distinct features of dendritic cells and anti-immunoglobulin activated B cells as stimulators of the primary mixed lymphocyte reaction
    • Metlay, J.P., Pure, H. and Steinman, R.M. Distinct features of dendritic cells and anti-immunoglobulin activated B cells as stimulators of the primary mixed lymphocyte reaction. J. Exp. Med. 1989, 169, 239-254.
    • (1989) J. Exp. Med. , vol.169 , pp. 239-254
    • Metlay, J.P.1    Pure, H.2    Steinman, R.M.3
  • 38
    • 0023735364 scopus 로고
    • Differential ability of B cell specific for external vs. internal influenza virus proteins to respond to help from influenza-specific T-cell clones in vivo
    • Scherle, P.A. and Gerhard, W. Differential ability of B cell specific for external vs. internal influenza virus proteins to respond to help from influenza-specific T-cell clones in vivo. Proc. Natl Acad. Sci. USA 1988, 85, 4446-4450.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4446-4450
    • Scherle, P.A.1    Gerhard, W.2
  • 39
    • 0025994286 scopus 로고
    • Activity of CD4+ T-cell clones of type 1 and type 2 in generation of influenza specific cytotoxic responses in vitro
    • Palladino, G., Scherle, P.A. and Gerhard, W. Activity of CD4+ T-cell clones of type 1 and type 2 in generation of influenza specific cytotoxic responses in vitro. J. Virol. 1991, 65, 6071-6076.
    • (1991) J. Virol. , vol.65 , pp. 6071-6076
    • Palladino, G.1    Scherle, P.A.2    Gerhard, W.3
  • 40
    • 0028840343 scopus 로고
    • Inactivated influenza virus, when presented on dendritic cells, elicits human CD8+ cytolytic T cell responses
    • Bender, A., Bui, L.K., Feldman, M.A.V., Larsoon, M. and Bhardwaj, N. Inactivated influenza virus, when presented on dendritic cells, elicits human CD8+ cytolytic T cell responses. J. Exp. Med. 1995, 182, 1663-1671.
    • (1995) J. Exp. Med. , vol.182 , pp. 1663-1671
    • Bender, A.1    Bui, L.K.2    Feldman, M.A.V.3    Larsoon, M.4    Bhardwaj, N.5
  • 43
    • 0025292252 scopus 로고
    • Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type I recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese Hamster Ovary cells
    • Leonard, C.K., Spellman, M.W., Riddle, L., Harris, R.J., Thomas, J.N. and Gregory, T.J. Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type I recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese Hamster Ovary cells. J. Biol. Chem. 1990, 265, 10373-10382.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3    Harris, R.J.4    Thomas, J.N.5    Gregory, T.J.6
  • 44
    • 0028982258 scopus 로고
    • Oocyte Galα1-3Gal epitopes implicated in sperm adhesion to the zona pellucida glycoprotein ZP3 are not required for fertilization in the mouse
    • Thall, A.D., Maly, P. and Lowe, J.B. Oocyte Galα1-3Gal epitopes implicated in sperm adhesion to the zona pellucida glycoprotein ZP3 are not required for fertilization in the mouse. J. Biol. Chem. 1995, 270, 21437-21442
    • (1995) J. Biol. Chem. , vol.270 , pp. 21437-21442
    • Thall, A.D.1    Maly, P.2    Lowe, J.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.